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Database: UniProt
Entry: E0N9L4_NEIME
LinkDB: E0N9L4_NEIME
Original site: E0N9L4_NEIME 
ID   E0N9L4_NEIME            Unreviewed;       741 AA.
AC   E0N9L4;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR009407};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR009407};
DE   AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|PIRNR:PIRNR009407};
GN   Name=icd {ECO:0000313|EMBL:EFM04324.1};
GN   ORFNames=HMPREF0602_1194 {ECO:0000313|EMBL:EFM04324.1};
OS   Neisseria meningitidis ATCC 13091.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=862513 {ECO:0000313|EMBL:EFM04324.1, ECO:0000313|Proteomes:UP000005526};
RN   [1] {ECO:0000313|EMBL:EFM04324.1, ECO:0000313|Proteomes:UP000005526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13091 {ECO:0000313|EMBL:EFM04324.1,
RC   ECO:0000313|Proteomes:UP000005526};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC         Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42;
CC         Evidence={ECO:0000256|PIRNR:PIRNR009407};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC       {ECO:0000256|PIRSR:PIRSR009407-3};
CC   -!- SIMILARITY: Belongs to the monomeric-type IDH family.
CC       {ECO:0000256|PIRNR:PIRNR009407}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFM04324.1}.
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DR   EMBL; AEEF01000061; EFM04324.1; -; Genomic_DNA.
DR   RefSeq; WP_002213820.1; NZ_GL397187.1.
DR   AlphaFoldDB; E0N9L4; -.
DR   HOGENOM; CLU_025308_1_0_4; -.
DR   Proteomes; UP000005526; Unassembled WGS sequence.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 2.
DR   InterPro; IPR004436; Isocitrate_DH_NADP_mono.
DR   NCBIfam; TIGR00178; monomer_idh; 1.
DR   PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR   PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR   Pfam; PF03971; IDH; 1.
DR   PIRSF; PIRSF009407; IDH_monmr; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Glyoxylate bypass {ECO:0000256|PIRNR:PIRNR009407};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR009407-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3};
KW   NADP {ECO:0000256|PIRNR:PIRNR009407, ECO:0000256|PIRSR:PIRSR009407-4};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407,
KW   ECO:0000313|EMBL:EFM04324.1};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         83..88
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         133..140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         136
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         351
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         548
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         549
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         553
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         585..586
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         590
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         601..603
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         650
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            256
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            421
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   741 AA;  80105 MW;  A2396A6D06B6A188 CRC64;
     MTQKSTIVYT HTDEAPALAT QSLLPIVQAF TRHADIDVKT ADISLSGRIL AAFPEYLTEA
     QRVPDALAEL GELVKQPDAN VIKLPNISAS VPQLTAAIKE LQSKGFAVPD YPADPQTDEE
     KVVRERYDRI KGSAVNPVLR EGNSDRRAPK AVKNFAKKNP HSMGAWTKDS KTHVATMQSG
     DFFHNEQSVT VPEATSVSIV FTDKQGNKKE LRAPVALKAG EIIDATVMSK KALLAFLAEQ
     VKDAKAKGVL FSLHMKATMM KVSDPIIFGH AVKVFFAPVF EKFGGKLAAA GVNVNNGFGN
     LLANLDKLDA DTRAAVEAEI AAVYAANPDL AMVDSDKGIT NLHVPSDVIV DASMPAMIRN
     SGRMWDKNGK AQDTKAVIPD SSYAGVYQAT IDFCREHGAF DPTTMGTVPN VGLMAQAAEE
     YGSHNKTFEI EADGQVQVID AEGKVLMQHD VEAGDIWRMC QTKDAPVKDW VQLAVNRARL
     SNTPAVFWLD ENRPHDKSLL AKVKAYLAEL DTNGLDIRVL APEEAAKFSL GRLKNGEDTI
     SVTGNVLRDY LTDLFPILEL GTSAKMLSIV PLMNGGGMFE TGAGGSAPKH VQQFLEENHL
     RWDSLGEFLA LAVSFEHLAQ KTGNAKAQVL ADTLDAATEK LLLNDKSPKR KAGELDNRGS
     HFYLTLYWAQ ELAAQDKDAE LKAAFTPLAA ALTADEAKIV AELSAVQGKA ADIGGYYAAN
     PEKAAQVMRP SVTFNQALNA L
//
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